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Intraflagellar Transport 57 Homolog (Chlamydomonas) Proteins (IFT57)

On www.antibodies-online.com are 8 Intraflagellar Transport 57 Homolog (Chlamydomonas) (IFT57) Proteins from 4 different suppliers available. Additionally we are shipping IFT57 Antibodies (86) and and many more products for this protein. A total of 100 IFT57 products are currently listed.

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novel transcription regulatory mechanism of REST by HIPPI may contribute to the deregulation of transcription observed in the cell model of Huntington disease.

Results show that pro-apoptotic Hippi-Hip-1 heterodimers can recruit procaspase-8 into a complex of Hippi, Hip-1 and procaspase-8, and launch apoptosis through components of the 'extrinsic' cell-death pathway.

Hip-1 and Hippi cooperate to induce neuronal apoptosis in a caspase-8-dependent manner.

Sonic hedgehog (Shh) pathway is downregulated in the neural tube in the absence of Hippi, which results in failure to establish ventral neural cell fate.

These findings suggest that Rybp and Hippi may functionally interact in the apoptotic processes that accompany normal murine neural development.

sequencing of IFT57 in 13 OFDS subjects and 12 subjects with Ellis-Van Creveld syndrome was negative. This report identifies the implication of IFT57 in human pathology and highlights the first description of a ciliary transport defect in OFDS, extending the genetic heterogeneity of this subgroup of ciliopathies.

novel transcription regulatory mechanism of REST by HIPPI may contribute to the deregulation of transcription observed in the cell model of Huntington disease.

Results show that pro-apoptotic Hippi-Hip-1 heterodimers can recruit procaspase-8 into a complex of Hippi, Hip-1 and procaspase-8, and launch apoptosis through components of the 'extrinsic' cell-death pathway.

critical for the death-promoting effects of mutant huntingtin protein in cultured cells

Hippi interacts with the viral death protein Apoptin.

Hippi expression induced apoptosis by releasing AIF and cytochrome c from mitochondria, activation of caspase-1 and caspase-3, and altering the expression of apoptotic genes and genes involved in mitochondrial complex I and II.

Crystals of the pDED of HIPPI were grown in space group P4(1), with unit-cell parameters a = b = 77.42, c = 33.31 A and a calculated Matthews coefficient of 1.88 A3 Da(-1) (33% solvent content) with two molecules per asymmetric unit.

In summary, we showed that HIPPI could interact with the putative promoter sequence of caspase-1 and increased the expression of the downstream gene suggesting that HIPPI could act as transcription regulator.

Over-expression of BLOC1S2 in presence or absence of HIPPI does not induce apoptosis. However, BLOC1S2 & HIPPI sensitize NCH89 glioblastoma cells to pro-apoptotic actions of staurosporine & death ligand TRAIL.

IFT57 Protein Profile

Protein Summary

Required for the formation of cilia. May also have pro- apoptotic function (By similarity).